Kinetic deuterium isotope effects in cytochrome P450 oxidation reactions

J Labelled Comp Radiopharm. 2013 Jul-Aug;56(9-10):428-31. doi: 10.1002/jlcr.3031. Epub 2013 Mar 10.

Abstract

Cytochrome P450 (P450) enzymes account for ~75% of the metabolism of drugs. Most of the reactions catalyzed by P450s are mixed-function oxidations, and a C-H bond is (usually) broken. The rate-limiting nature of this step can be analyzed using the kinetic isotope effect (KIE) approach. The most relevant type of KIE is one termed intermolecular non-competitive, indicative of rate-limiting C-H bond breaking. A plot of KIE versus kcat for several P450s showed a correlation coefficient (r(2) ) of 0.62. Deuterium substitution has been considered as a potential means of slowing drug metabolism or redirecting sites of metabolism in some cases, and several general points can be made regarding the potential for application of deuterium in drug design/development based on what is known about P450 KIEs.

Keywords: bond energy; cytochrome P450; dealkylation reactions; drugs; isotope effects; kinetics; oxidations.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Cytochrome P-450 Enzyme System / chemistry*
  • Deuterium / chemistry*
  • Drug Discovery
  • Humans
  • Kinetics
  • Oxidation-Reduction

Substances

  • Cytochrome P-450 Enzyme System
  • Deuterium